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Expert Opinion on Therapeutic Patents Volume 12, 2002 - Issue 5
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Miscellaneous

Therapeutic developments in matrix metalloproteinase inhibition

Prediman K Shah Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
,
Douglas J Wilkin Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
,
Terence M Doherty Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
,
Hiroyasu Uzui Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
,
Tripathi B Rajavashisth Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
,
Kamlesh Asotra Atherosclerosis Research Centre, Division of Cardiology, Department of Medicine, and the Burns and Allen Research Institute, Cedars-Sinai Medical Centre and UCLA School of Medicine, Los Angeles, California 90048, USA
&
Duanqing Pei Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455-0217, USA
 show all
Pages 665-707 | Published online: 25 Feb 2005

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  • •Not especially pertinent to MMPs, but an excellent review of osteoblast development by several widely recognised authorities.
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  • •Like reference 6, not especially pertinent to MMPs, but an excellent review of osteoclast development by a noted expert in the field.
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  • ••An important and well-written paperaccompanying reference 9.
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  • ••A very recent overview of the history ofMMP research that nicely summarises the major findings of four decades of MMP research.
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  • ••A widely-cited review on MT-MMPs thatis essential reading for those interested in this MMP subfamily, and in MMPs and MMPIs in general.
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  • ••An excellent and widely cited reviewdetailing in particular the molecular mechanisms of MMP activation.
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  • ••Several well-known authors in the MMPfield review the important role of MT-MMPs in tissue invasion, with particular reference to tumour growth and metastatic processes, a prominent focus of research in MT-MMPs.
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  • ••An excellent landmark paper that focuseson an area of MMP metabolism that is poorly understood but the subject of intense interest, namely post-translational processing of nascent MMPs from the trans-Golgi network to their ultimate fate.
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  • •A well-written paper dealing with specific aspects of MMP processing.
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  • ••One of the first papers documenting theexistence of membrane-associated MMPs, now known to comprise a six-member subfamily that is thought to be particulary central to proteolytic ECM degradation.
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  • ••A detailed study on the molecularmechanisms of proMMP-2 activation by MT1-MMP that adds more evidence for a central role for MT-MMPs in regulating a pericellular proteolytic cascade and controlling directed, focal ECM degradation.
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  • ••An excellent review on the endogenous inhibitors of MMPs (TIMPs).
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  • ••A good general review of the role ofproteases in homeostatic and pathologic processes, particularly inflammation-associated conditions.
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  • AMOUR A, KNIGHT CG, WEBSTER A et al: The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. (2000) 473:275–279.
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  • ••An excellent paper describing an aspect ofprotease processing that is receiving increasing interest and is the focus of therapeutic drug development efforts.
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  • •This report details developments in therapeutic inhibition of TACE, and is a good companion to reference 50.
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  • ••An excellent, expert review on the role ofadhesion receptors in angiogenesis by two prominent authorities in adhesion receptor (integrin) physiology and molecular biology.
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  • •An intriguing recent report concerning manipulation of TIMP expression and activity as a therapeutic strategy.
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  • ••A very good synopsis of the role of TIMPsin processes such as apoptosis that are not directly related to ECM degradation. Highlights some aspects of the considerable complexity of TIMP expression and function.
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  • BAKER AH, GEORGE SJ, ZALTSMAN AB, MURPHY G, NEWBY AC: Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. Br .j Cancer (1999) 79:1347–1355.
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  • GEORGE SJ, LLOYD CT, ANGELINI GD, NEWBY AC, BAKER AH: Inhibition of late vein graft neointima formation in human and porcine models by adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-3. Circulation (2000) 101:296–304.
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  • ••An excellent review and a primaryreference source for studies on general proteolysis and inhibition of proteolysis.
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  • ••An early paper on a topic that is not well understood, but might become a fruitful area for therapeutic drug discovery, namely membrane-associated events in MMP metabolic processes.
  • OH J, TAKAHASHI R, KONDO S etal.: The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Cell (2001) 107:789–800.
  • ••An excellent recent paper concerningmembrane-associated events in the regulation of ECM remodelling and degradation by MMPs.
  • WEAVER VM: Membrane-associated mmp regulators. Novel cell adhesion tumor suppressor proteins? Dev. Cell (2002) 2:6–7.
  • LIJNEN HR, VAN HOEF B, COLLEN D: Inactivation of the serpin a2-antiplasmin by stromelysin-1. Biochim. Biophys. Acta. (2001) 1547:206–213.
  • LIU Z, ZHOU X, SHAPIRO SD et al.: The serpin alphal-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in viva Cell (2000) 102:647–655.
  • MAST AE, ENGHILD JJ, NAGASE H, SUZUKI K, PIZZO SV, SALVESEN G: Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J. Biol. Chem. (1991) 266:15810–15816.
  • BIRKEDAL-HANSEN H, MOORE WG, BODDEN MK et al.: Matrix metalloproteinases: a review. Grit. Rev Oral Biol. Med (1993) 4:197–250.
  • SPRINGMAN EB, ANGLETON EL, BIRKEDAL-HANSEN H, VAN WART HE: Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a cysteine switch' mechanism for activation. Proc. Nati Acad. Sci. USA (1990) 87:364–368.
  • WOESSNER JF Jr.: Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB (1991) 5:2145–2154.
  • ••A classic early review on MMPs andTIMPs, frequently cited.
  • JACKSON C, NGUYEN M, ARKELL J, SAMBROOK P etal.: Selective matrix metalloproteinase (MMP) inhibition in rheumatoid arthritis-targetting gelatinase A activation. Irillamm. Res. (2001) 50:183–186.
  • LEGRAND C, POLETTE M, TOURNIER JM et al.: uPA/plasmin system-mediated MMP-9 activation is implicated in bronchial epithelial cell migration. Exp. Cell Res. (2001) 264:326–336.
  • LUNEN HR: Plasmin and matrix metalloproteinases in vascular remodeling. Thromb. Haemost. (2001) 86:324–333.
  • ••An excellent recent review on the role ofproteases in vascular biology including, but not limited to, MMPs.
  • HU B, KAPILA YL, BUDDHIKOT M, SHIGA M, KAPILA S: Coordinate induction of collagenase-1, stromelysin-1 and urokinase plasminogen activator (uPA) by the 120-kDa cell-binding fibronectin fragment in fibrocartilaginous cells: uPA contributes to activation of procollagenase-1. Matrix Biol. (2000) 19:657–669.
  • FESTUCCIA C, DOLO V, GUERRA F et al.: Plasminogen activator system modulates invasive capacity and proliferation in prostatic tumor cells. CM]. Exp. Metastasis (1998) 16:513–528.
  • LUNEN HR, SILENCE J, VAN HOEF B, COLLEN D: Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice. Blood (1998) 91:2045–2053.
  • BARAMOVA EN, BAJOU K, REMACLE A et al.: Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation. FEBS Lett. (1997) 405:157–162.
  • KESKI-OJA J, LOHI J, TUUTTILA A, TRYGGVASON K, VARTIO T: Proteolytic processing of the 72,000-Da Type IV collagenase by urokinase plasminogen activator. Exp. Cell Res. (1992) 202:471–476.
  • SORSA T, SALO T, KOIVUNEN E et al.: Activation of Type IV procollagenases by human tumor-associated trypsin-2. _J. Biol. Chem. (1997) 272:21067–21074.
  • NGUYEN M, ARKELL J, JACKSON CJ: Thrombin rapidly and efficiently activates gelatinase A in human microvascular endothelial cells via a mechanism independent of active MT1 matrix metalloproteinase. Lab. Invest. (1999) 79:467–475.
  • NGUYEN M, ARKELL J, JACKSON CJ. Activated protein C directly activates human endothelial gelatinase A. J. Biol. Chem. (2000) 275:9095–9098.
  • JOHNSON JL, JACKSON CL, ANGELINI GD, GEORGE SJ: Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques. Arterioscler. Thromb. Vasc. Biol. (1998) 18:1707–1715.
  • •Describes the role of MMPs in atherosclerotic plaque development and destabilisation, as well as other cardiovascular diseases associated with disordered ECM remodelling.
  • LEES M, TAYLOR DJ, WOOLLEY DE: Mast cell proteinases activate precursor forms of collagenase and stromelysin, but not of gelatinases A and B. Eur. j Biochem. (1994) 223:171–177.
  • CARMELIET P, MOONS L, LUNEN R eta].: Urokinase-generated plasmin activates matrix metalloproteinases during aneurysm formation. Nat. Genet. (1997) 17:439–444.
  • •An important and often cited paper documenting a role for MMP dysregulation in arterial aneurysm formation.
  • ROUIS M, ADAMY C, DUVERGER N eta].: Adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-1 reduces atherosclerotic lesions in apolipoprotein E-deficient mice. Circulation (1999) 100:533–540.
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  • ••A short but excellent review on MMPs,very widely referenced.
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  • ••This review is a nice complement toreference 113. An excellent introduction.
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  • ••Another excellent review on MMPs and a source for primary references in the field.
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  • HERNANDEZ-BARRANTES S, TOTH M, BERNARDO MM et al: Binding of143.active (57 kDa) membrane Type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro- MIV1P-2 activation. J. Biol. Chem. (2000)144.275: 12080–12089.
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  • PEI D: Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MIVIP. J. Biol. Chem. (1999) 274:8925–8932.
  • •A good paper and one of the first reports on MT5-MMP.
  • WANG Y, JOHNSON AR, YE QZ, DYER RD: Catalytic activities and substrate specificity of the human membrane Type 4 matrix metalloproteinase catalytic domain. J. Biol. Chem. (1999) 274:33043–33049.
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  • SHOFUDA K, YASUMITSU H, NISHIHASHI A, MIKI K, MIYAZAKI K: Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain. _J. Biol. Chem. (1997) 272:9749–9754.
  • ••One of the early papers implicating animportant role for the membrane-associated MMPs in vascular biology and pathology.
  • MIYAMORI H, TAKINO T, KOBAYASHI Y et al.: Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases. J. Biol. Chem. (2001) 276:28204–28211.
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  • STEINER DF: The proprotein convertases. Curr. Opin Chem. Biol. (1998) 2:31–39.
  • ••An excellent review on the proteinsinvolved in post-translational processing of nascent MMPs. This area of MMP biology is currently active and may lead to important therapeutic drug discoveries.
  • NAKAYAMA K: Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. (1997) 327:625–635.
  • SEIDAH NG, CHRETIEN M: Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. (1999) 848:45–62.
  • ••A good review on proprotein convertasesthat participate in post-translational processing and activation of MMPs.
  • CHRETIEN M, MBIKAY M, GASPAR L, SEIDAH NG: Proprotein convertases and the pathophysiology of human diseases: prospective considerations. Proc. Assoc. Am. Physicians (1995) 107:47–66.
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  • HIDALGO M, ECKHARDT SG: Development of matrix metalloproteinase inhibitors in cancer therapy. J. Nat. Cancer Inst. (2001) 93:178–193.
  • ••A very good overview of developments inMMP inhibition as a treatment paradigm for tumour development and, especially, metastasis.
  • QUARANTA V: Cell migration through extracellular matrix: membrane-type metalloproteinases make the way. J. Cell. Biol. (2000) 149:1167–1169.
  • ••A provocative and well-writtencommentary outlining the potential central role that the MT-MMPs play in the MMP-mediated matrix remodelling and degradation.
  • DUNSMORE SE, SAARIALHO-KERE UK, ROBY JD et al.: Matrilysin expression and function in airway epithelium. J. Clin. Invest. (1998) 102:1321–1331.
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  • KAHARI VM, SAARIALHO-KERE U: Matrix metalloproteinases and their inhibitors in tumour growth and invasion. Ann. Med (1999) 31:34–45.
  • ••Widely quoted work on MMPparticipation in tumour growth and metastatic processes, and relevant therapeutic drug development efforts.
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  • ••Excellent description of the various levelsat which MMP expression and activity are regulated.
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  • ••A first-rate comprehensive review, and anexcellent source for primary references.
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  • ••An up-to-date appraisal of the currentstatus of progress in understanding the role of MMPs in cardiovascular disorders, with particular reference to atherogenesis and plaque stability.
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  • •This paper clearly implicates an important role for MT3-MMP in atherosclerotic plaque composition and stability.
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  • •A report on the role of MT1-MMP in atherosclerotic plaque development.
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  • •• An excellent and comprehensive treatment of the many genetically altered murine MMP knockout and transgenic genotypes, and their utility in various models of disease.
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  • •• This is the first report on the MT1-MMPdeficient mouse genotype, the only MTMMP knockout mutation produced to date. A fundamental role for MT1-MMP in diverse biological processes is clearly demonstrated.
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  • •• This review summarises progress in the development of drugs to inhibit MMPs as a treatment for cancer and metastasis.
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  • GEORGE SJ: Therapeutic potential of matrix metalloproteinase inhibitors in atherosclerosis. Expert Opin. Investig. Drugs (2000) 9(5):993–1007.
  • •• A timely report on the growing field of MMP inhibition as a treatment for cardiovascular diseases, particularly atherosclerotic disease.
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  • •• A classic must-read reference on the role of MMPs in cardiovascular diseases of various types.
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  • ••Excellent report on the involvement ofMMPs in chronic obstructive pulmonary disease.
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  • •This paper pertains to an area of MMP research that will likely see accelerating research and development interest: dysregulated MMP expression and activity in ventricular remodelling following myocardial infarction.
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  • •An early paper describing conformational changes in the MMP-inhibitor complex that led to the development of new compounds to inhibit MMPs.
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  • YAMAMOTO M, IKEDA S, KONDO H, INOUE S: Design and synthesis of dual inhibitors for matrix metalloproteinase and cathepsin. Bioorg. Med. Chem. Lett. (2002) 12:375–378.
  • •A recent update on efforts to produce protease inhibitors.
  • BROWN PD: Ongoing trials with matrix metalloproteinase inhibitors. Expert Opin. Investig. Drugs (2000) 9(9):2167–2177.
  • ••This excellent report details the successesand, unfortunately, failures in the clinical trials involving MMPIs, largely in oncology.
  • COUSSENS LM, FINGLETON B, MATRISIAN LM: Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science (2002) 295:2387-2392. An excellent recent review on the use of MMPIs in clinical trials of various cancers.
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  • ••A thorough review of the role of MMPs intumour growth and metastasis.
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  • ••Another good review on the participationof MMPs in tissue invasion.
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  • •An intriguing recent report concerning manipulation of TIMP expression and activity as a therapeutic strategy.
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  • •One of the early reports on the clinical development of batimastat, an early MMPI that was subsequently tested further in several clinical trials.
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  • •An interesting report concerning the participation of dysregulated MMP involvement in arthritic pathologies. This is likely to be an area of considerable further research and development efforts.
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  • LEE RT: Matrix metalloproteinase inhibition and the prevention of heart failure. Trends Cardiovasc. Med (2001) 11:202–205.
  • ••A concise review of the participation ofdisordered MMP expression and activity in heart failure and myocardial remodelling processes.
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